Purification and characterization of novel truncated fragments of bioactive proteins from porcine intestine with effects on insulin secretion

During purification of porcine gut polypeptides with respect to glucose-induced insulin secretion from pancreatic β cells, two novel fragments of the known gastrointestinal peptides were isolated and chemically characterized. They are truncated forms of phosphatidylethanolamine-binding protein (PEBP93-124) and valosin (Valosin3-25). These novel fragments, Valosin3-25 and PEBP93-124, showed stimulatory activities on glucose-induced insulin secretion from pancreatic β cells. That the novel fragments had their respective bioactivities imply that these novel peptide-fragments could be the novel processed peptide-forms in organism. Therefore, isolation and chemical characterization of bioactive peptides from natural materials in the post genomic and bio-informational era are still necessary and will help scientist to have deeper insight into proteomics. In addition, these purified porcine gut polypeptides may provide an option to the treatment of Diabetes and also bring limelight to the mechanism of Diabetes manifestation. Keywords: Insulin, truncated peptide, phosphatidylethanolanmine binding protein, valosin, glucose-dependent insulinotropic polypeptide.